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Simultaneous purification and reversible immobilization of d-amino acid oxidase from Trigonopsis variabilis on a hydrophobic support

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Abstract

Purification and reversible immobilization of d-amino acid oxidase from Trigonopsis variabilis could be simultaneously accomplished by hydrophobic interaction on Phenyl Sepharose CL-4B in the presence of 50 mM pyrophosphate buffer (pH 8.5). The presence of a high salt concentration of 2M, which is generally required for the hydrophobic interactions, was not essential for the hydrophobic immobilization. The enzyme in free as well as immobilized form was optimally active between pH 7.0 and 9.0. The immobilized preparation could be reused in a batch process for the conversion of d-amino acids to α-keto acids. When the activity of the preparation dropped below practical limits, the gel could be regenerated by water wash and recharged with fresh crude extract from yeast.

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Authors and Affiliations

  1. Nuclear Agriculture and Biotechnology Division, Bhabha Atomic Research Centre, 400085, Trombay, Mumbai, India

    Stanislaus F. D’Souza & Ashwini Deshpande

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  1. Stanislaus F. D’Souza
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  2. Ashwini Deshpande
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Correspondence to Stanislaus F. D’Souza.

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D’Souza, S.F., Deshpande, A. Simultaneous purification and reversible immobilization of d-amino acid oxidase from Trigonopsis variabilis on a hydrophobic support. Appl Biochem Biotechnol 95, 83–92 (2001). https://doi.org/10.1385/ABAB:95:2:083

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  • DOI: https://doi.org/10.1385/ABAB:95:2:083

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